Optimized oxidoreductases for medium and large scale industrial biotransformations
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publications
Total records: 126
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[ 2019 ] Linde D, Ayuso-Fernández I, Ruiz-Dueñas FJ, Martínez AT Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan Arch. Biochem. Biophys., 668: 23-28
[ 2019 ] Serrano A, Sancho F, Viña-Gonzalez J, Carro J, Alcalde M, Guallar V, Martínez AT Switching the substrate preference of fungal aryl-alcohol oxidase: towards stereoselective oxidation of secondary benzyl alcohols Catal. Sci. Technol., doi: 10.1039/C8CY02447B
[ 2019 ] Viña-Gonzalez J, Jimenez-Lalana D, Sancho F, Serrano A, Martínez AT, Guallar V, Alcalde M Structure‐Guided Evolution of Aryl Alcohol Oxidase from Pleurotus eryngii for the Selective Oxidation of Secondary Benzyl Alcohols Adv. Synth. Catal., 361: 2514-2525
[ 2018 ] Carro J, Fernandez-Fueyo E, Fernández-Alonso C, Cañada J, Ullrich R, Hofrichter M, Alcalde M, Ferreira P, Martínez AT Self-sustained enzymatic cascade for the production of 2,5-furandicarboxylic acid from 5-methoxymethylfurfural Biotechnol. Biofuels, 11: 86-96
[ 2018 ] Carro J, Ferreira P, Martínez AT, Gadda G Stepwise Hydrogen Atom and Proton Transfers in Dioxygen Reduction by Aryl-Alcohol Oxidase Biochemistry, doi: 10.1021/acs.biochem.8b00106
[ 2018 ] Ewing TA, Kühn J, Segarra S, Tortajada M, Zuhse R, van Berkel WJ Multigram Scale Enzymatic Synthesis of (R)‐1‐(4′‐Hydroxyphenyl)ethanol Using Vanillyl Alcohol Oxidase Adv. Synth. Catal., 360: 2370-2376
year2019
Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan
Linde D, Ayuso-Fernández I, Ruiz-Dueñas FJ, Martínez AT
Arch. Biochem. Biophys., 668: 23-28

Dye-decolorizing peroxidase (DyP) from Auricularia auricula-judae and versatile peroxidase (VP) from Pleurotus eryngii oxidize the three mononitrophenol isomers. Both enzymes have been overexpressed in Escherichia coli and in vitro activated. Despite their very different three-dimensional structures, the nitrophenol oxidation site is located at a solvent-exposed aromatic residue in both DyP (Trp377) and VP (Trp164), as revealed by liquid chromatography coupled to mass spectrometry and kinetic analyses of nitrophenol oxidation by the native enzymes and their tryptophan-less variants (the latter showing 10–60 fold lower catalytic efficiencies).

Download the article for free until July 5th on: https://authors.elsevier.com/a/1Z3YPw0NEPWp

Official webpage of indox [ industrialoxidoreductases ]. Optimized oxidoreductases for medium and large scale industrial biotransformations. This project has received funding from the European Union’s Seventh Framework Programme for research, technological development and demonstration under Grant Agreement nº: FP7-KBBE-2013-7-613549. © indox 2013. Developed by garcíarincón